Angiotensin I Converting Enzyme-Inhibitory Peptides from Wine

摘要

Six peptides that inhibit angiotensin I converting enzyme (ACE) were fractionated and purified from Muscat Bailey A red (Bailey × Muscat Hamburg) wine. Muscat Bailey A wine was concentrated to 1/2 of its original volume, then applied to a reverse phase open column. Peptides were eluted using a stepwise gradient of 0 to 90/100 ethanol. The fraction that eluted at 10/100 ethanol was the most inhibitory. Peptides in this fraction were separated into three active compound fractions (I, II, and III) by gel filtration on Toyopearl HW-40. These fractions were further separated by reverse-phase HPLC on a μBondasphere C_(18) column, using a linear gradient of 0 to 50/100 acetonitrile into six peptides that inhibited ACE. The amino acid sequences and IC_(50) values (concentration required for 50/100 ACE inhibition) of the purified peptides were LIPPGVPY (17.5 μM), YYAPFDGIL (83.0 μM), YYAPF (26.4 μM), SWSF (76.3 μM), WVPSVY (25.7 μM), and AWPF (18.3 μM).